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G3P_CORGL
ID   G3P_CORGL               Reviewed;         334 AA.
AC   Q01651;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83};
DE            Short=GAPDH {ECO:0000250|UniProtKB:P9WN83};
DE            EC=1.2.1.12 {ECO:0000250|UniProtKB:P9WN83};
DE   AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83};
GN   Name=gap; OrderedLocusNames=Cgl1588, cg1791;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX   PubMed=1400158; DOI=10.1128/jb.174.19.6076-6086.1992;
RA   Eikmanns B.J.;
RT   "Identification, sequence analysis, and expression of a Corynebacterium
RT   glutamicum gene cluster encoding the three glycolytic enzymes
RT   glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and
RT   triosephosphate isomerase.";
RL   J. Bacteriol. 174:6076-6086(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC       phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC       NAD. The first reaction step involves the formation of a hemiacetal
CC       intermediate between G3P and a cysteine residue, and this hemiacetal
CC       intermediate is then oxidized to a thioester, with concomitant
CC       reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC       second NAD, and the thioester is attacked by a nucleophilic inorganic
CC       phosphate to produce BPG. {ECO:0000250|UniProtKB:P9WN83}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000250|UniProtKB:P9WN83};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P54226}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X59403; CAA42045.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98981.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21596.1; -; Genomic_DNA.
DR   PIR; A43260; A43260.
DR   RefSeq; NP_600802.1; NC_003450.3.
DR   RefSeq; WP_003862250.1; NC_006958.1.
DR   AlphaFoldDB; Q01651; -.
DR   SMR; Q01651; -.
DR   STRING; 196627.cg1791; -.
DR   World-2DPAGE; 0001:Q01651; -.
DR   PRIDE; Q01651; -.
DR   KEGG; cgb:cg1791; -.
DR   KEGG; cgl:Cgl1588; -.
DR   PATRIC; fig|196627.13.peg.1550; -.
DR   eggNOG; COG0057; Bacteria.
DR   HOGENOM; CLU_030140_0_2_11; -.
DR   OMA; HETYKGE; -.
DR   BRENDA; 1.2.1.12; 960.
DR   BRENDA; 1.2.1.59; 960.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43148; PTHR43148; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; NAD; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..334
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000145647"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         12..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         152..154
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         183
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         198
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         211..212
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         234
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         315
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   SITE            180
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   CONFLICT        25..26
FT                   /note="SD -> NG (in Ref. 1; CAA42045)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        333..334
FT                   /note="KL -> QALN (in Ref. 1; CAA42045)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  36046 MW;  33792AF65FA90FA7 CRC64;
     MTIRVGINGF GRIGRNFFRA VLERSDDLEV VAVNDLTDNK TLSTLLKFDS IMGRLGQEVE
     YDDDSITVGG KRIAVYAERD PKNLDWAAHN VDIVIESTGF FTDANAAKAH IEAGAKKVII
     SAPASNEDAT FVYGVNHESY DPENHNVISG ASCTTNCLAP MAKVLNDKFG IENGLMTTVH
     AYTGDQRLHD APHRDLRRAR AAAVNIVPTS TGAAKAVALV LPELKGKLDG YALRVPVITG
     SATDLTFNTK SEVTVESINA AIKEAAVGEF GETLAYSEEP LVSTDIVHDS HGSIFDAGLT
     KVSGNTVKVV SWYDNEWGYT CQLLRLTELV ASKL
 
 
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